Cell entry by enveloped viruses: redox considerations for HIV and SARS-coronavirus.
Identifieur interne : 001D87 ( PubMed/Curation ); précédent : 001D86; suivant : 001D88Cell entry by enveloped viruses: redox considerations for HIV and SARS-coronavirus.
Auteurs : Emmanuel Fenouillet [France] ; Rym Barbouche ; Ian M. JonesSource :
- Antioxidants & redox signaling [ 1523-0864 ] ; 2007.
Descripteurs français
- KwdFr :
- Animaux, Disulfures (), Données de séquences moléculaires, Humains, Infections à VIH (anatomopathologie), Infections à VIH (métabolisme), Modèles biologiques, Motifs d'acides aminés, Oxydoréduction, Protéine d'enveloppe gp120 du VIH (métabolisme), Protéine d'enveloppe gp41 du VIH (métabolisme), Structure tertiaire des protéines, Séquence d'acides aminés, VIH (Virus de l'Immunodéficience Humaine) (métabolisme), Virus du SRAS (métabolisme).
- MESH :
- anatomopathologie : Infections à VIH.
- métabolisme : Infections à VIH, Protéine d'enveloppe gp120 du VIH, Protéine d'enveloppe gp41 du VIH, VIH (Virus de l'Immunodéficience Humaine), Virus du SRAS.
- Animaux, Disulfures, Données de séquences moléculaires, Humains, Modèles biologiques, Motifs d'acides aminés, Oxydoréduction, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Animals, CD4 Antigens (biosynthesis), Disulfides (chemistry), HIV (metabolism), HIV Envelope Protein gp120 (metabolism), HIV Envelope Protein gp41 (metabolism), HIV Infections (metabolism), HIV Infections (pathology), Humans, Models, Biological, Molecular Sequence Data, Oxidation-Reduction, Protein Structure, Tertiary, SARS Virus (metabolism).
- MESH :
- chemical , biosynthesis : CD4 Antigens.
- chemical , chemistry : Disulfides.
- metabolism : HIV, HIV Envelope Protein gp120, HIV Envelope Protein gp41, HIV Infections, SARS Virus.
- pathology : HIV Infections.
- Amino Acid Motifs, Amino Acid Sequence, Animals, Humans, Models, Biological, Molecular Sequence Data, Oxidation-Reduction, Protein Structure, Tertiary.
Abstract
For enveloped viruses, genome entry into the target cell involves two major steps: virion binding to the cell-surface receptor and fusion of the virion and cell membranes. Virus-cell membrane fusion is mediated by the virus envelope complex, and its fusogenicity is the result of an active virus-cell interaction process that induces conformation changes within the envelope. For some viruses, such as influenza, exposure to an acidic milieu within the cell during the early steps of infection triggers the necessary structural changes. However, for other pathogens which are not exposed to such environmental stress, activation of fusogenicity can result from precise thiol/disulfide rearrangements mediated by either an endogenous redox autocatalytic isomerase or a cell-associated oxidoreductase. Study of the activation of HIV envelope fusogenicity has revealed new knowledge about how redox changes within a viral envelope trigger fusion. We discuss these findings and their implication for anti-HIV therapy. In addition, to compare and contrast the situation outlined for HIV with an enveloped virus that can fuse with the cell plasma membrane independent of the redox status of its envelope protein, we review parallel data obtained on SARS coronavirus entry.
DOI: 10.1089/ars.2007.1639
PubMed: 17567241
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Virus-cell membrane fusion is mediated by the virus envelope complex, and its fusogenicity is the result of an active virus-cell interaction process that induces conformation changes within the envelope. For some viruses, such as influenza, exposure to an acidic milieu within the cell during the early steps of infection triggers the necessary structural changes. However, for other pathogens which are not exposed to such environmental stress, activation of fusogenicity can result from precise thiol/disulfide rearrangements mediated by either an endogenous redox autocatalytic isomerase or a cell-associated oxidoreductase. Study of the activation of HIV envelope fusogenicity has revealed new knowledge about how redox changes within a viral envelope trigger fusion. We discuss these findings and their implication for anti-HIV therapy. In addition, to compare and contrast the situation outlined for HIV with an enveloped virus that can fuse with the cell plasma membrane independent of the redox status of its envelope protein, we review parallel data obtained on SARS coronavirus entry.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17567241</PMID><DateCompleted><Year>2007</Year><Month>09</Month><Day>14</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1523-0864</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>8</Issue><PubDate><Year>2007</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid. Redox Signal.</ISOAbbreviation></Journal><ArticleTitle>Cell entry by enveloped viruses: redox considerations for HIV and SARS-coronavirus.</ArticleTitle><Pagination><MedlinePgn>1009-34</MedlinePgn></Pagination><Abstract><AbstractText>For enveloped viruses, genome entry into the target cell involves two major steps: virion binding to the cell-surface receptor and fusion of the virion and cell membranes. Virus-cell membrane fusion is mediated by the virus envelope complex, and its fusogenicity is the result of an active virus-cell interaction process that induces conformation changes within the envelope. For some viruses, such as influenza, exposure to an acidic milieu within the cell during the early steps of infection triggers the necessary structural changes. However, for other pathogens which are not exposed to such environmental stress, activation of fusogenicity can result from precise thiol/disulfide rearrangements mediated by either an endogenous redox autocatalytic isomerase or a cell-associated oxidoreductase. Study of the activation of HIV envelope fusogenicity has revealed new knowledge about how redox changes within a viral envelope trigger fusion. We discuss these findings and their implication for anti-HIV therapy. 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